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000053707 084__ $$2WoS$$aMultidisciplinary Sciences
000053707 1001_ $$0P:(DE-HGF)0$$aBudyak, I. L.$$b0
000053707 245__ $$aShape and oligomerization state of the cytoplasmic domain of the phototaxis transducer II from Natronobacterium pharaonis
000053707 260__ $$aWashington, DC$$bAcademy$$c2006
000053707 300__ $$a15428 - 15433
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000053707 520__ $$aPhototaxis allows archaea to adjust flagellar motion in response to light. In the photophobic response of Natronobacterium pharaonis, light-activated sensory rhodopsin II causes conformational changes in the transducer II protein (pHtrII), initiating the two-component signaling system analogous to bacterial chemotaxis. pHtrII's cytoplasmic domain (pHtrII-cyt) is homologous to the cytoplasmic domains of eubacterial chemotaxis receptors. Chemotaxis receptors require dimerization for activity and are in vivo-organized in large clusters. In this study we investigated the oligomerization and aggregation states of pHtrII-cyt by using chemical cross-linking, analytical gel-filtration chromatography, and small-angle neutron scattering. We show that pHtrII-cyt is monomeric in dilute buffers, but forms dimers in 4 M KCl, the physiological salt concentration for halophilic archaea. At high ammonium sulfate concentration, the protein forms higher-order aggregates. The monomeric protein has a rod-like shape, 202 A in length and 14.4 A in diameter; upon dimerization the length increases to 248 A and the diameter to 18.2 A. These results suggest that under high salt concentration the shape and oligomerization state of pHtrII-cyt are comparable to those of chemotaxis receptors.
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000053707 536__ $$0G:(DE-Juel1)FUEK415$$aGroßgeräte für die Forschung mit Photonen, Neutronen und Ionen (PNI)$$cP55$$x2
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000053707 65320 $$2Author$$aarchaebacteria
000053707 65320 $$2Author$$adynamics
000053707 65320 $$2Author$$ahalophilic
000053707 65320 $$2Author$$asmall-angle neutron scattering
000053707 650_2 $$2MeSH$$aArchaeal Proteins: chemistry
000053707 650_2 $$2MeSH$$aArchaeal Proteins: genetics
000053707 650_2 $$2MeSH$$aArchaeal Proteins: metabolism
000053707 650_2 $$2MeSH$$aBiopolymers: chemistry
000053707 650_2 $$2MeSH$$aCarotenoids: chemistry
000053707 650_2 $$2MeSH$$aCarotenoids: genetics
000053707 650_2 $$2MeSH$$aCarotenoids: metabolism
000053707 650_2 $$2MeSH$$aCross-Linking Reagents: chemistry
000053707 650_2 $$2MeSH$$aCrystallography, X-Ray
000053707 650_2 $$2MeSH$$aDimerization
000053707 650_2 $$2MeSH$$aLight
000053707 650_2 $$2MeSH$$aNatronobacterium: chemistry
000053707 650_2 $$2MeSH$$aNatronobacterium: metabolism
000053707 650_2 $$2MeSH$$aParticle Size
000053707 650_2 $$2MeSH$$aPhototrophic Processes: physiology
000053707 650_2 $$2MeSH$$aProtein Structure, Quaternary
000053707 650_2 $$2MeSH$$aProtein Structure, Tertiary
000053707 650_7 $$00$$2NLM Chemicals$$aArchaeal Proteins
000053707 650_7 $$00$$2NLM Chemicals$$aBiopolymers
000053707 650_7 $$00$$2NLM Chemicals$$aCross-Linking Reagents
000053707 650_7 $$00$$2NLM Chemicals$$aphototaxis receptor sensory rhodopsin II, Natronobacterium pharaonis
000053707 650_7 $$036-88-4$$2NLM Chemicals$$aCarotenoids
000053707 650_7 $$2WoSType$$aJ
000053707 7001_ $$0P:(DE-Juel1)VDB4339$$aPipich, V.$$b1$$uFZJ
000053707 7001_ $$0P:(DE-HGF)0$$aMironova, O. S.$$b2
000053707 7001_ $$0P:(DE-HGF)0$$aSchlesinger, R.$$b3
000053707 7001_ $$0P:(DE-HGF)0$$aZaccai, G.$$b4
000053707 7001_ $$0P:(DE-HGF)0$$aKlein-Seetharaman, J.$$b5
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